scholarly journals Iron Reduction and Trans Plasma Membrane Electron Transfer in the Yeast Saccharomyces cerevisiae

1992 ◽  
Vol 100 (2) ◽  
pp. 769-777 ◽  
Author(s):  
Emmanuel Lesuisse ◽  
Pierre Labbe
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Electron Transfer ◽  
Plasma Membrane ◽  
Iron Reduction ◽  
Yeast Saccharomyces Cerevisiae

scholarly journals The a-factor transporter (STE6 gene product) and cell polarity in the yeast Saccharomyces cerevisiae.

1993 ◽  
Vol 120 (5) ◽  
pp. 1203-1215 ◽  
Author(s):  
K Kuchler ◽  
H G Dohlman ◽  
J Thorner
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Plasma Membrane ◽  
Gene Product ◽  
Cell Polarity ◽  
Polyclonal Antibodies ◽  
Apparent Molecular Weight ◽  
Subcellular Fractionation ◽  
Mating Pheromone ◽  
Yeast Saccharomyces Cerevisiae ◽  
Factor Secretion

STE6 gene product is required for secretion of the lipopeptide mating pheromone a-factor by Saccharomyces cerevisiae MATa cells. Radiolabeling and immunoprecipitation, either with specific polyclonal antibodies raised against a TrpE-Ste6 fusion protein or with mAbs that recognize c-myc epitopes in fully functional epitope-tagged Ste6 derivatives, demonstrated that Ste6 is a 145-kD phosphoprotein. Subcellular fractionation, various extraction procedures, and immunoblotting showed that Ste6 is an intrinsic plasma membrane-associated protein. The apparent molecular weight of Ste6 was unaffected by tunicamycin treatment, and the radiolabeled protein did not bind to concanavalin A, indicating that Ste6 is not glycosylated and that glycosylation is not required either for its membrane delivery or its function. The amino acid sequence of Ste6 predicts two ATP-binding folds; correspondingly, Ste6 was photoaffinity-labeled specifically with 8-azido-[alpha-32P]ATP. Indirect immunofluorescence revealed that in exponentially growing MATa cells, the majority of Ste6 showed a patchy distribution within the plasma membrane, but a significant fraction was found concentrated in a number of vesicle-like bodies subtending the plasma membrane. In contrast, in MATa cells exposed to the mating pheromone alpha-factor, which markedly induced Ste6 production, the majority of Ste6 was incorporated into the plasma membrane within the growing tip of the elongating cells. The highly localized insertion of this transporter may establish pronounced anisotropy in a-factor secretion from the MATa cell, and thereby may contribute to the establishment of the cell polarity which restricts partner selection and cell fusion during mating to one MAT alpha cell.

scholarly journals Cell surface recycling in yeast: mechanisms and machineries

2016 ◽  
Vol 44 (2) ◽  
pp. 474-478 ◽  
Author(s):  
Chris MacDonald ◽  
Robert C. Piper
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Plasma Membrane ◽  
Membrane Protein ◽  
Cell Surface ◽  
Mammalian Cells ◽  
Genetic System ◽  
Integral Membrane Protein ◽  
Protein Activity ◽  
Yeast Saccharomyces Cerevisiae ◽  
Central Process

Sorting internalized proteins and lipids back to the cell surface controls the supply of molecules throughout the cell and regulates integral membrane protein activity at the surface. One central process in mammalian cells is the transit of cargo from endosomes back to the plasma membrane (PM) directly, along a route that bypasses retrograde movement to the Golgi. Despite recognition of this pathway for decades we are only beginning to understand the machinery controlling this overall process. The budding yeast Saccharomyces cerevisiae, a stalwart genetic system, has been routinely used to identify fundamental proteins and their modes of action in conserved trafficking pathways. However, the study of cell surface recycling from endosomes in yeast is hampered by difficulties that obscure visualization of the pathway. Here we briefly discuss how recycling is likely a more prevalent process in yeast than is widely appreciated and how tools might be built to better study the pathway.

scholarly journals ATP-sensitive K+ channels in a plasma membrane H+-ATPase mutant of the yeast Saccharomyces cerevisiae.

1989 ◽  
Vol 86 (20) ◽  
pp. 7866-7870 ◽  
Author(s):  
J. A. Ramirez ◽  
V. Vacata ◽  
J. H. McCusker ◽  
J. E. Haber ◽  
R. K. Mortimer ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Plasma Membrane ◽  
Yeast Saccharomyces Cerevisiae ◽  
K Channels

scholarly journals Carbonyl cyanide m-chlorophenylhydrazone induced calcium signaling and activation of plasma membrane H+-ATPase in the yeast Saccharomyces cerevisiae

2008 ◽  
Vol 8 (4) ◽  
pp. 622-630 ◽  
Author(s):  
Michele B.P. Pereira ◽  
Renata Tisi ◽  
Luciano G. Fietto ◽  
Anamaria S. Cardoso ◽  
Mônica M. França ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Plasma Membrane ◽  
Calcium Signaling ◽  
Yeast Saccharomyces Cerevisiae ◽  
Carbonyl Cyanide

scholarly journals The RA Domain of Ste50 Adaptor Protein Is Required for Delivery of Ste11 to the Plasma Membrane in the Filamentous Growth Signaling Pathway of the Yeast Saccharomyces cerevisiae

2006 ◽  
Vol 26 (3) ◽  
pp. 912-928 ◽  
Author(s):  
Dagmar M. Truckses ◽  
Joshua E. Bloomekatz ◽  
Jeremy Thorner
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Plasma Membrane ◽  
Protein Kinase ◽  
Adaptor Protein ◽  
Mitogen Activated Protein Kinase ◽  
Invasive Growth ◽  
Pheromone Response ◽  
Yeast Saccharomyces Cerevisiae ◽  
Mapk Kinase

ABSTRACT In Saccharomyces cerevisiae, pheromone response requires Ste5 scaffold protein, which ensures efficient G-protein-dependent recruitment of mitogen-activated protein kinase (MAPK) cascade components Ste11 (MAPK kinase kinase), Ste7 (MAPK kinase), and Fus3 (MAPK) to the plasma membrane for activation by Ste20 protein kinase. Ste20, which phosphorylates Ste11 to initiate signaling, is activated by binding to Cdc42 GTPase (membrane anchored via its C-terminal geranylgeranylation). Less clear is how activated and membrane-localized Ste20 contacts Ste11 to trigger invasive growth signaling, which also requires Ste7 and the MAPK Kss1, but not Ste5. Ste50 protein associates constitutively via an N-terminal sterile-alpha motif domain with Ste11, and this interaction is required for optimal invasive growth and hyperosmotic stress (high-osmolarity glycerol [HOG]) signaling but has a lesser role in pheromone response. We show that a conserved C-terminal, so-called “Ras association” (RA) domain in Ste50 is also essential for invasive growth and HOG signaling in vivo. In vitro the Ste50 RA domain is not able to associate with Ras2, but it does associate with Cdc42 and binds to a different face than does Ste20. RA domain function can be replaced by the nine C-terminal, plasma membrane-targeting residues (KKSKKCAIL) of Cdc42, and membrane-targeted Ste50 also suppresses the signaling deficiency of cdc42 alleles specifically defective in invasive growth. Thus, Ste50 serves as an adaptor to tether Ste11 to the plasma membrane and can do so via association with Cdc42, thereby permitting the encounter of Ste11 with activated Ste20.

Electron transfer constituents in plasma membrane fractions of Avena sativa and Saccharomyces cerevisiae

1984 ◽  
Vol 34 (1-2) ◽  
pp. 103-110 ◽  
Author(s):  
Juan M. Ramirez ◽  
Guillermo Gimenez Gallego ◽  
Ramon Serrano
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Electron Transfer ◽  
Plasma Membrane ◽  
Avena Sativa

Localization of a 210-kDa microtubule-interacting protein in the yeast Saccharomyces cerevisiae

1992 ◽  
Vol 38 (2) ◽  
pp. 149-152 ◽  
Author(s):  
J. Hašek ◽  
J. Jochová ◽  
P. Dráber ◽  
V. Viklický ◽  
E. Streiblová
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Cycle ◽  
Monoclonal Antibody ◽  
Plasma Membrane ◽  
Key Words ◽  
Budding Yeast ◽  
Yeast Saccharomyces Cerevisiae ◽  
Double Labeling ◽  
Interacting Protein ◽  
Cytoplasmic Microtubules

Using the monoclonal antibody MA-01, which recognizes a 210-kDa protein in cell-free extracts, spindle and cytoplasmic microtubules were visualized in budding yeast, Saccharomyces cerevisiae. In additional, a spot-like staining was found beneath the plasma membrane, revealing in part correlation with F-actin distribution. This pattern was common for cells of all cell-cycle stages. The interaction of the protein recognized by MA-01 with microtubules was confirmed in the double labeling with a polyclonal antitubulin antibody and by the sensitivity of intranuclear structures stained by MA-01 to the microtubule disrupting drug nocodazole. Key words: immunoblotting, immunofluorescence, microtubule-interacting protein, Saccharomyces cerevisiae.

scholarly journals Clathrin adaptors mediate two sequential pathways of intra-Golgi recycling

2021 ◽  
Vol 221 (1) ◽  
Author(s):  
Jason C. Casler ◽  
Natalie Johnson ◽  
Adam H. Krahn ◽  
Areti Pantazopoulou ◽  
Kasey J. Day ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Plasma Membrane ◽  
Golgi Apparatus ◽  
Transmembrane Proteins ◽  
Membrane Traffic ◽  
Yeast Saccharomyces Cerevisiae ◽  
Clathrin Adaptor ◽  
Pass Through ◽  
Kinetics Of

The pathways of membrane traffic within the Golgi apparatus are not fully known. This question was addressed using the yeast Saccharomyces cerevisiae, in which the maturation of individual Golgi cisternae can be visualized. We recently proposed that the AP-1 clathrin adaptor mediates intra-Golgi recycling late in the process of cisternal maturation. Here, we demonstrate that AP-1 cooperates with the Ent5 clathrin adaptor to recycle a set of Golgi transmembrane proteins, including some that were previously thought to pass through endosomes. This recycling can be detected by removing AP-1 and Ent5, thereby diverting the AP-1/Ent5–dependent Golgi proteins into an alternative recycling loop that involves traffic to the plasma membrane followed by endocytosis. Unexpectedly, various AP-1/Ent5–dependent Golgi proteins show either intermediate or late kinetics of residence in maturing cisternae. We infer that the AP-1/Ent5 pair mediates two sequential intra-Golgi recycling pathways that define two classes of Golgi proteins. This insight can explain the polarized distribution of transmembrane proteins in the Golgi.

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